A5E6Y5 (A5E6Y5_LODEL) Unreviewed, UniProtKB/TrEMBL
Last modified
November 16, 2011.
Version 32.
History...
Names and origin
| Protein names | Submitted name: D-arabinono-1,4-lactone oxidase EMBL EDK47193.1 | ||
| Gene names |
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| Organism | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome] | ||
| Taxonomic identifier | 379508 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Lodderomyces |
Protein attributes
| Sequence length | 564 AA. |
| Sequence status | Complete. |
| Protein existence | Predicted |
Ontologies
| Keywords | |
|---|---|
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | membrane Inferred from electronic annotation. Source: InterPro |
| Molecular function | D-arabinono-1,4-lactone oxidase activity Inferred from electronic annotation. Source: InterPro UDP-N-acetylmuramate dehydrogenase activityInferred from electronic annotation. Source: InterPro flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. Cuomo C.A.Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239 and ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CH981532 Genomic DNA. Translation: EDK47193.1. |
| RefSeq | XP_001523528.1. XM_001523478.1. |
3D structure databases | |
| ProteinModelPortal | A5E6Y5. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5230524. |
| KEGG | lel:LELG_05374. |
Phylogenomic databases | |
| OMA | DCLFSQF. |
| OrthoDB | EOG4GF6PD. |
Family and domain databases | |
| InterPro | IPR007173. ALO. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR010031. FAD_lactone_oxidase. IPR023595. LGO_GLO. IPR006094. Oxid_FAD_bind_N. IPR006093. Oxy_OxRdtase_FAD_BS. [Graphical view] |
| Gene3D | G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit. |
| KO | K00107. |
| Pfam | PF04030. ALO. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view] |
| PIRSF | PIRSF000136. LGO_GLO. 1 hit. |
| SUPFAM | SSF56176. FAD-binding_2. 1 hit. |
| TIGRFAMs | TIGR01678. FAD_lactone_ox. 1 hit. |
| PROSITE | PS51387. FAD_PCMH. 1 hit. PS00862. OX2_COVAL_FAD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | A5E6Y5_LODEL | ||||||||
| Accession | Primary (citable) accession number: A5E6Y5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
